Insight into the Stereocontrol of DNA Polymerase-Catalysed Reaction by Chiral Cobalt Complexes

Enantiomers of chiral substances typically have distinct biological activities, thus, the explorations of biochemical processes at the enantiomeric level has very high significance. This study investigated DNA polymerase-catalyzed reaction modulated by various types of chiral cobalt complexes. The experimental data showed that polymerase reactions were inhibited or accelerated in the presence of K[Co(edta)] center dot 2H(2)O or [Co(en)(3)]I-3 center dot H2O. More importantly, the stereocontrol of bioreactivity was found to be different for the enantiomers, which was reflected in their ability to bind to the polymerase reaction system. The docking simulation illustrated that the acceleration or inhibition of polymerase reaction could be correlated with diverse electrostatic energy induced by the attached metal chelates, whereas the different stereocontrol of bioreactivity for the enantiomers was attributed to a discrepancy of Van der Waals interactions between the enantiomer and polymerase catalytic sites.

Automated summary

Enantiomers of chiral substances possess different biological activities, making it crucial to explore biochemical processes at the enantiomeric level. This study investigated the DNA polymerase-catalyzed reaction controlled by various types of chiral cobalt complexes and found that the enantiomers exhibited different stereocontrol of bioreactivity, which could be attributed to diverse electrostatic energy induced by the attached metal chelates and discrepancies in Van der Waals interactions between the enantiomer and polymerase catalytic sites.